Interaction of isoliquiritigenin with bovine serum albumin studied by fluorescence quenching method

doi:10.5246/jcps.2016.03.023

Journal of Chinese Pharmaceutical Sciences ›› 2016, Vol. 25 ›› Issue (3): 196-200.DOI: 10.5246/jcps.2016.03.023

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Interaction of isoliquiritigenin with bovine serum albumin studied by fluorescence quenching method

Bo Han¹, Fei Long¹, Wei Yu¹, Wen Chen^1*, Xinchun Wang¹, Gang Guo², Liangxue Zhou²

1. School of Pharmacy, Shihezi University, Shihezi 832002, China
2. State Key Laboratory of Biotherapy and Cancer Center, and Department of Neurosurgery, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China

Received:2015-10-29 Revised:2015-11-27 Online:2016-03-29 Published:2015-12-15
Contact: Tel.: 0993-2057010, E-mail: chen-wen2000@126.com
Supported by:
National Natural Science Foundation of China (Grant No. 81560699), Scientific and Technological Project of the Science and Technology Department of Guangdong Province (Grant No. 2014A020209026), Social Development Research and Technology Transfer Program (Grant No. 2015AD002), Outstanding Young Scientific Personnel Training Plan of Shihezi University (Grant No. 2015-ZRKXJQ08).

Abstract

Abstract:

Interaction of ioliquiritigenin (ISL), which is the main active component of a commonly used traditional Chinese medicine (TCM) Glycyrrhiza uralensis Fisch. with bovine serum albumin (BSA) has been investigated. The quenching mechanism of fluorescence of bovine serum albumin by ISL was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters ΔH⁰, ΔG⁰, ΔS⁰ at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (ISL) was obtained according to Förster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.

Key words: Isoliquiritigenin, Bovine serum albumin, Thermodynamic parameters, Energy transfer

CLC Number:

R917

Supporting:

Bo Han, Fei Long, Wei Yu, Wen Chen, Xinchun Wang, Gang Guo, Liangxue Zhou. Interaction of isoliquiritigenin with bovine serum albumin studied by fluorescence quenching method[J]. Journal of Chinese Pharmaceutical Sciences, 2016, 25(3): 196-200.

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Interaction of isoliquiritigenin with bovine serum albumin studied by fluorescence quenching method

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